L-alloisocitrate dehydrogenase and oxalosuccinate decarboxylase from a Pseudomonas sp. utilizing L-alloisocitrate

Katsuya Gomi, Teruhiko Beppu, Kei Arima

Research output: Contribution to journalArticlepeer-review

5 Citations (Scopus)

Abstract

Two novel enzymes, NAD+-linked L-alloisocitrate (erythro-Ls-isocitrate) dehydrogenase and oxalosuccinate decarboxylase, were found and purified from a strain of Pseudomonas isolated as an L-alloisocitrate utilizing bacterium. The former enzyme catalyzes a reversible oxidation-reduction between L-alloisocitrate and oxalosuccinate which favors oxalosuccinate reduction. The latter enzyme catalyzes rapid decarboxylation of oxalosuccinate to α-ketoglutarate and CO2. Both enzymes require no metals for their activities. Complete oxidative decarboxylation of L-alloisocitrate to α-ketoglutarate occurs as a result of the sequential reactions catalyzed by these two enzymes. L-Alloisocitrate induces both enzymes in the growing pseudomonad.

Original languageEnglish
Pages (from-to)1439-1448
Number of pages10
JournalJournal of biochemistry
Volume87
Issue number5
DOIs
Publication statusPublished - 1980 Jan 1
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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